How calcium makes endocytic receptors attractive

作者：Andersen Christian B F; Moestrup Soren K^*

来源：TRENDS IN BIOCHEMICAL SCIENCES, 2014, 39(2): 82-90.

DOI：10.1016/j.tibs.2013.12.003

Nutrients, biological waste-products, toxins, pathogens, and other ligands for endocytosis are typically captured by multidomain receptors with multiligand specificity. Upon internalization, the receptor-ligand complex segregates, followed by lysosomal degradation of the ligand and recycling of the receptor. Endosomal acidification and calcium efflux lead to the essential ligand-receptor affinity switch and separation. Recent data, including crystal structures of receptor-ligand complexes, now reveal how calcium, in different types of domain scaffolds, functions in a common way as a removable 'lynchpin' that stabilizes favorable positioning of ligand-attractive receptor residues. In addition to explaining how calcium depletion can cause ligand-receptor dissociation, the new data add further insight into how acidification contributes to dissociation through structural changes that affect the receptor calcium sites.

• 出版日期2014-2